100 SKIN CARE
Benefits of recombinant type XVII collagen
Li Jiaji, Wang Liping, Ji Baihui, Cao Kaijie, Feng Peiying, Fu Shengwei - Trautec
An important biological protein with unique properties, collagen is used in many fields such as the chemical industry, medicine, food and cosmetics.1
The collagen sold currently
on the market is mainly animal-sourced. However, during the processing of acid, base, or enzymatic extraction methods, a native structure of collagen is basically destroyed, and the protein is severely degraded, resulting in sharply decreased bioactivity. What is more, animal-sourced collagen is
heterogeneous mixture of polypeptides with different sizes,2
and the significant batch-
to-batch difference can lead to unstable qualities of final products. In addition to the risk of associated infectious diseases brought by animals, such as bovine spongiform encephalopathy, animal-derived collagen may also cause immune hypersensitivity when consumed by humans.3-5 Human collagen type XVII is a
transmembrane non-fibroblast collagen, which is a homogeneous trimer composed of three identical α1 (XVII) chains and is divided into three major domains: intracellular, transmembrane, and extracellular domains.6 Collagen type XVII is a component of hemidesmosomes in cells and plays an important role in the interaction between epithelial cells and a basement membrane. It can regulate the cellular adhesion, separation, development, and is important for the differentiation and regeneration of keratinocytes. Besides, maintenance of collagen type XVII in stem cells is critical for orchestrating skin homeostasis and preventing hair follicle ageing.7,8 However, unlike collagen type I and type
III, which are abundant in both human beings and animals, collagen type XVII is traceable in these two species, making it impossible to be mass-produced even by extraction method. With the development of biotechnology, some types of recombinant human collagen have been plentifully produced. Compared with animal collagen, recombinant human collagen obtained from fermentation is animal-free and thus can eliminate the safety problems caused by animals. Moreover, recombinant human collagen
can be highly bioactive and is usually highly or totally homologous to native human collagen through rational amino acid design. To our knowledge, although many companies realized large-scale production of recombinant human
PERSONAL CARE March 2024
collagen type I and type III, scale production of recombinant collagen type XVII has not been reported yet. Here, we have successfully achieved scale
production of recombinant collagen type XVII by fermentation with Pichia pastoris and the trade name of this product is SRHC Type XVII. The molecular weight of SRHC Type XVII is 23.8-kDa and the homology degree with human collagen type XVII is >90%. Next, we carried some cell experiments
and adopted an ex vivo skin model to evaluate the efficacy of SRHC Type XVII as a new raw material for cosmetics, finding that the treatment of SRHC Type XVII can achieve the following. ■ Promote cell migration and adhesion ■ Increase the expression level of fundamental proteins involved in basement membrane ■ Repair dermal–epidermal junction (DEJ)damage and significantly increase the endogenous expression level of collagen type XVII both at the transcriptional and translational level Therefore, we believe that SRHC Type XVII
can be used as a novel and attractive raw material for cosmetics.
Amino acid sequence design and chassis cell selection for SRHC Type XVII production To generate a highly bioactive recombinant collagen type XVII, we firstly referred to some published papers related with human collagen type XVII and found that there are many atypical active integrin binding sites- Lys- Gly-Asp (KGD) motifs on the COL15 domain of human collagen type XVII.9 The KGD motif can promote integrin-
mediated cell spreading by binding with α5β1 and αVβ1 integrin. In addition to KGD motifs, we also take some other points into consideration like other integrin binding sites, stability of the protein and the feasibility of secretory strategy. Thus, the resultant amino acid sequence
of SRHC Type XVII is composed of five regions from native human collagen type XVII and containing up to ten active KGD sites. In addition, we added Strep-Tag II tag to the N-terminal sequence and 6×His tag to the
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